- 著者
-
MORITA Shimpei
FUKASE Masami
HOSHINO Kumiko
FUKUDA Yoichi
YAMAGUCHI Masami
MORITA Yuhei
- 出版者
- Japanese Society of Plant Physiologists
- 雑誌
- Plant and cell physiology (ISSN:00320781)
- 巻号頁・発行日
- vol.35, no.7, pp.1049-1056, 1994-10
- 参考文献数
- 38
- 被引用文献数
-
6
A proteolytic activity directed against the a subunit of β-conglycinin was detected in resting mature seeds of the soybean [Glycine max (L.) Merrill] cultivar Keburi. The relationship between pH and activity and the effect of protease inhibitors revealed that the enzyme was a neutral/alkaline serine protease. The proteolysis of the a subunit of β-conglycinin yielded a specific product with a molecular weight of about 47,000, as determined by SDS-PAGE, but the enzyme had no activity against the β subunit. The amino acid composition, the molecular weight and the amino-terminal amino acid sequence of the proteolytic product revealed that the action of the enzyme on the a subunit was specific, with cleavage occurring only at the R126-R127 peptide bond of the a subunit. These characteristics of the protease indicate that the enzyme is a novel protease that has not previously been recognized in soybean seeds.